CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006348
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family D member 1 
Protein Synonyms/Alias
 Adrenoleukodystrophy protein; ALDP 
Gene Name
 ABCD1 
Gene Synonyms/Alias
 ALD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
64ASGVAAAKAGMNRVFubiquitination[1]
264VLRAFSPKFGELVAEubiquitination[2]
407ERIMSSYKEVTELAGubiquitination[2, 3]
462VRVEGPLKIRGQVVDubiquitination[2]
533TYGGVLYKPPPQRMFubiquitination[2, 3]
569SVEDMQRKGYSEQDLubiquitination[1, 2]
648GKIFQAAKDAGIALLubiquitination[1]
696RLSLTEEKQRLEQQLubiquitination[2]
708QQLAGIPKMQRRLQEubiquitination[4, 5]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Probable transporter. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity. 
Sequence Annotation
 DOMAIN 94 386 ABC transmembrane type-1.
 DOMAIN 474 700 ABC transporter.
 NP_BIND 507 514 ATP (By similarity).
 REGION 67 186 Interaction with PEX19.
 MOD_RES 733 733 Phosphoserine.
 CARBOHYD 214 214 N-linked (GlcNAc...) (Potential).  
Keyword
 ATP-binding; Complete proteome; Disease mutation; Glycoprotein; Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 745 AA 
Protein Sequence
MPVLSRPRPW RGNTLKRTAV LLALAAYGAH KVYPLVRQCL APARGLQAPA GEPTQEASGV 60
AAAKAGMNRV FLQRLLWLLR LLFPRVLCRE TGLLALHSAA LVSRTFLSVY VARLDGRLAR 120
CIVRKDPRAF GWQLLQWLLI ALPATFVNSA IRYLEGQLAL SFRSRLVAHA YRLYFSQQTY 180
YRVSNMDGRL RNPDQSLTED VVAFAASVAH LYSNLTKPLL DVAVTSYTLL RAARSRGAGT 240
AWPSAIAGLV VFLTANVLRA FSPKFGELVA EEARRKGELR YMHSRVVANS EEIAFYGGHE 300
VELALLQRSY QDLASQINLI LLERLWYVML EQFLMKYVWS ASGLLMVAVP IITATGYSES 360
DAEAVKKAAL EKKEEELVSE RTEAFTIARN LLTAAADAIE RIMSSYKEVT ELAGYTARVH 420
EMFQVFEDVQ RCHFKRPREL EDAQAGSGTI GRSGVRVEGP LKIRGQVVDV EQGIICENIP 480
IVTPSGEVVV ASLNIRVEEG MHLLITGPNG CGKSSLFRIL GGLWPTYGGV LYKPPPQRMF 540
YIPQRPYMSV GSLRDQVIYP DSVEDMQRKG YSEQDLEAIL DVVHLHHILQ REGGWEAMCD 600
WKDVLSGGEK QRIGMARMFY HRPKYALLDE CTSAVSIDVE GKIFQAAKDA GIALLSITHR 660
PSLWKYHTHL LQFDGEGGWK FEKLDSAARL SLTEEKQRLE QQLAGIPKMQ RRLQELCQIL 720
GEAVAPAHVP APSPQGPGGL QGAST 745 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005779; C:integral to peroxisomal membrane; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; NAS:UniProtKB.
 GO:0005325; F:peroxisomal fatty-acyl-CoA transporter activity; IGI:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
 GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
 GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
 GO:0042758; P:long-chain fatty acid catabolic process; IGI:UniProtKB.
 GO:0015919; P:peroxisomal membrane transport; NAS:UniProtKB.
 GO:0007031; P:peroxisome organization; IDA:UniProtKB.
 GO:0042760; P:very long-chain fatty acid catabolic process; IDA:UniProtKB. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR010509; ABC_Ald_N.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR017940; ABC_transporter_type1.
 IPR005283; FA_transporter.
 IPR027417; P-loop_NTPase. 
Pfam
 PF06472; ABC_membrane_2
 PF00005; ABC_tran 
SMART
 SM00382; AAA 
PROSITE
 PS50929; ABC_TM1F
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS